Protein target profile

VK055_4398

sulfite reductase (NADPH) hemoprotein, beta-component

Genome: KpATCC43816 Gene: cysI AIK82941.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GXH1

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Length 570

Pocket druggability 0.921

Metabolic reactions 1

Chokepoint No

Direct ligand evidence 0 55 total records

Functional annotation 1 EC 13 GO

Target summary

Strong target candidate with converging metabolic, structural and chemical evidence.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

Central metabolic position More central than 96.7% of genes in this genome. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Review the complete evidence below

Risks to review

Evidence coverage

Core evidence streams are available for this target.

Terms and data sources used on this page

PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.

AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.

ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.

pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.

FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.

Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.

PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.

ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.

ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.

LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.

Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.

DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.

Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.

EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.

KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.

Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.

Prioritization evidence

Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.

Off-target risk

Human off-target: No hit
Gut microbiome similarity: 3.2% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 35.413 Higher values support similarity to known essential genes.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 95.43 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

FPocket 0.921

Structure A0A0H3GXH1

Pocket Pocket 27

P2Rank 0.967

Structure A0A0H3GXH1

Pocket Pocket 1

ColabFold model

FPocket 0.903 · Pocket 27

P2Rank 0.948 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 151 / 4744 genomes with a hit

Prevalence 3.2%

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Sequence

UniProt A0A0H3GXH1

Pathways

KEGG R00858 BioCyc SULFITE-REDUCT-RXN

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

Explore metabolic network

Metabolic context: more central than 96.7% of genes in this genome, no human homolog detected.

Relative network centrality 96.7% more central than 96.7% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MSEKHPGPLVVEGKLSDAERMKLESNYLRGTIAEDLNDGLTGGFKGDNFLLIRFHGMYQQDDRDIRAERAAQKLEPRHAMLLRCRLPGGVITTTQWKAIDKFAAENTIYGSIRLTNRQTFQFHGILKKNVKPVHQMLHSVGLDALATANDMNRNVLCTSNPYESQLHAEAYEWAKKISEHLLPRTRAYAEIWLDQKKVATTDEEPILGQTYLPRKFKTTVVIPPQNDIDLHANDMNFVAIAENGKLVGFNLLVGGGLSIEHGNKKTYARTASEFGYLPLEHTLAVAEAVVTTQRDWGNRTDRKNAKTKYTLERVGVETFKAEVERRAGIKFEPIRPYEFTGRGDRIGWVKGIDDKWHLTLFIENGRILDYPGRPLKTGLLEIAKVHQGEFRITANQNLIVASVPEDQKARIEKLARDHGLMNAVTPQRENSMACVSFPTCPLAMAEAERFLPSFIDKVEGVMSKHGVSDEHIVTRVTGCPNGCGRAMLAEVGLVGKAPGRYNLHIGGNRNGTRIPRMYRENITESEILDSLDELVGRWAKEREAGEGFGDFTVRAGIIRPVLDPARDFWE

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 13 GO

Enzyme Commission (EC)

1.8.1.2

Gene Ontology (GO)

GO:0008652 The chemical reactions and pathways resulting in the formation of amino acids, organic acids containing one or more amino substituents.
GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
GO:0050661 Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.
GO:0051539 Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
GO:0020037 Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
GO:0004783 Catalysis of the reaction: hydrogen sulfide + 3 NADP+ + 3 H2O = sulfite + 3 NADPH + 3 H+.
GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.
GO:0009337 A multisubunit iron flavoprotein, which in yeast is composed of 2 alpha and 2 beta subunits. Catalyzes the reduction of sulfite to sulfide.
GO:0046872 Binding to a metal ion.
GO:0050311 Catalysis of the reaction: hydrogen sulfide + 3 oxidized ferredoxin + 3 H2O = sulfite + 3 reduced ferredoxin.
GO:0019344 The chemical reactions and pathways resulting in the formation of L-cysteine, 2-amino-3-mercaptopropanoic acid.
GO:0070814 The chemical reactions and pathways resulting in the formation of hydrogen sulfide, H2S.
GO:0000103 The pathways by which inorganic sulfate is processed and incorporated into sulfated compounds.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

32 records

Show feature table

Start	End	DB	Term	Name
425	567	Gene3D	G3DSA:3.30.413.10	Sulfite Reductase Hemoprotein, domain 1
425	567	InterPro	IPR045854	Nitrite and sulphite reductase 4Fe-4S domain-like superfamily
429	447	PRINTS	PR00397	Sirohaem Fe-binding site signature
429	447	InterPro	IPR006066	Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site
477	495	PRINTS	PR00397	Sirohaem Fe-binding site signature
477	495	InterPro	IPR006066	Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site
10	570	Hamap	MF_01540	Sulfite reductase [NADPH] hemoprotein beta-component [cysI].
10	570	InterPro	IPR011786	Sulphite reductase (NADPH) hemoprotein, beta subunit
148	340	FunFam	G3DSA:3.30.413.10:FF:000004	Sulfite reductase [NADPH] hemoprotein beta-component
150	344	SUPERFAMILY	SSF56014	Nitrite and sulphite reductase 4Fe-4S domain-like
150	344	InterPro	IPR045854	Nitrite and sulphite reductase 4Fe-4S domain-like superfamily
13	142	SUPERFAMILY	SSF55124	Nitrite/Sulfite reductase N-terminal domain-like
13	142	InterPro	IPR036136	Nitrite/Sulfite reductase ferredoxin-like domain superfamily
346	422	SUPERFAMILY	SSF55124	Nitrite/Sulfite reductase N-terminal domain-like
346	422	InterPro	IPR036136	Nitrite/Sulfite reductase ferredoxin-like domain superfamily
428	559	SUPERFAMILY	SSF56014	Nitrite and sulphite reductase 4Fe-4S domain-like
428	559	InterPro	IPR045854	Nitrite and sulphite reductase 4Fe-4S domain-like superfamily
173	331	Pfam	PF01077	Nitrite and sulphite reductase 4Fe-4S domain
173	331	InterPro	IPR006067	Nitrite/sulphite reductase 4Fe-4S domain
425	567	FunFam	G3DSA:3.30.413.10:FF:000003	Sulfite reductase [NADPH] hemoprotein beta-component
19	558	NCBIfam	TIGR02041	assimilatory sulfite reductase (NADPH) hemoprotein subunit
19	558	InterPro	IPR011786	Sulphite reductase (NADPH) hemoprotein, beta subunit
148	340	Gene3D	G3DSA:3.30.413.10	Sulfite Reductase Hemoprotein, domain 1
148	340	InterPro	IPR045854	Nitrite and sulphite reductase 4Fe-4S domain-like superfamily
12	565	PANTHER	PTHR11493	SULFITE REDUCTASE [NADPH] SUBUNIT BETA-RELATED
12	565	InterPro	IPR045169	Nitrite and sulphite reductase 4Fe-4S domain containing protein
353	416	Pfam	PF03460	Nitrite/Sulfite reductase ferredoxin-like half domain
353	416	InterPro	IPR005117	Nitrite/Sulfite reductase ferredoxin-like domain
81	138	Pfam	PF03460	Nitrite/Sulfite reductase ferredoxin-like half domain
81	138	InterPro	IPR005117	Nitrite/Sulfite reductase ferredoxin-like domain
477	493	ProSitePatterns	PS00365	Nitrite and sulfite reductases iron-sulfur/siroheme-binding site.
477	493	InterPro	IPR006066	Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site

3D structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.

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Pocket score High Medium Low

How colors and pocket overlays are used

Uniform protein color marks the displayed model as a single molecular object.

Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.

Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.

'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.

'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.

'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.

Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · FPocket

Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #27

0.921

Likely same site as P2Rank 1 3.9 Å 28 shared residues 80% of smaller site

Unusual size

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.967

Likely same site as FPocket 27 3.9 Å 28 shared residues 80% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.251

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Surrounding area

Site 3 P2Rank #3

0.148

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Surrounding area

Site 4 P2Rank #4

0.048

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Surrounding area

Site 5 P2Rank #5

0.018

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Surrounding area

Residue sets

UniProt: Binding site:434-434

UniProt: Binding site:440-440

UniProt: Binding site:479-479

UniProt: Binding site:483-483

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.948

Likely same site as FPocket 27 3.3 Å 21 shared residues 78% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.043

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Surrounding area

Site 3 P2Rank #3

0.043

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Surrounding area

Site 4 P2Rank #4

0.006

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Surrounding area

Site 5 P2Rank #5

0.006

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Surrounding area

All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold DB AF_A0A0H3GXH1	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_4398	ColabFold	—	—	full sequence	—	Loaded

Ligand evidence

Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.

55 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 5 records from similar proteins

Structural ligands 5 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

CMO PDB via homolog 28.0 Da · LogP -0.04 · TPSA 19.9 Open detail RCSB PDB

FES PDB via homolog Detail RCSB PDB

HOA PDB via homolog Detail RCSB PDB

NO2 PDB via homolog Detail RCSB PDB

SX PDB via homolog Detail RCSB PDB

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in Target, use Open crystal to inspect it in the structure viewer.

No PDB structure with a co-crystallized ligand found for this exact protein.

Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.

Ligand	Source crystal	UniProt (homolog)	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CMO RCSB PDB	5GEP	P17846	28.0 Da LogP -0.04 TPSA 19.9	✓ Ro5	✓ Clean	`[C-]#[O+]`
FES RCSB PDB	5H8Y	O23813	175.8 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]S[Fe]1`
HOA RCSB PDB	3VKT	Q76KB0	33.0 Da LogP -0.67 TPSA 46.2	✓ Ro5	✓ Clean	`NO`
NO2 RCSB PDB	3GEO	P17846	46.0 Da LogP 0.25 TPSA 52.5	✓ Ro5	✓ Clean	`N(=O)[O-]`
SX RCSB PDB	7GEP	P17846	48.1 Da LogP -0.34 TPSA 17.1	✓ Ro5	✓ Clean	`O=S`

Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL bioactivity data found for this exact protein.

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL hits found through similar proteins.

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC403598 ZINC	0.800	273.3 Da LogP 2.14 TPSA 92.8	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(Oc2ccc(O)cc2)cc1)C(=O)O`
ZINC403599 ZINC	0.800	273.3 Da LogP 2.14 TPSA 92.8	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(Oc2ccc(O)cc2)cc1)C(=O)O`
ZINC39351856 ZINC	0.741	328.4 Da LogP 1.26 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(-c2ccc(C[C@H](N)C(=O)O)cc2)cc1)C…`
ZINC32333 ZINC	0.690	244.1 Da LogP 1.40 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(Br)cc1)C(=O)O`
ZINC32334 ZINC	0.690	244.1 Da LogP 1.40 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(Br)cc1)C(=O)O`
ZINC3679925 ZINC	0.690	291.1 Da LogP 1.25 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(I)cc1)C(=O)O`
ZINC391104 ZINC	0.690	291.1 Da LogP 1.25 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(I)cc1)C(=O)O`
ZINC4202286 ZINC	0.690	209.2 Da LogP 0.34 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(C(=O)O)cc1)C(=O)O`
ZINC4202287 ZINC	0.690	209.2 Da LogP 0.34 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(C(=O)O)cc1)C(=O)O`
ZINC6092920 ZINC	0.690	223.2 Da LogP 0.27 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(CC(=O)O)cc1)C(=O)O`
ZINC6506146 ZINC	0.690	223.2 Da LogP 0.27 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(CC(=O)O)cc1)C(=O)O`
ZINC34319489 ZINC	0.688	231.3 Da LogP 1.50 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc2cc(O)ccc2c1)C(=O)O`
ZINC34319490 ZINC	0.688	231.3 Da LogP 1.50 TPSA 83.5	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc2cc(O)ccc2c1)C(=O)O`
ZINC2512061 ZINC	0.677	360.4 Da LogP 0.67 TPSA 167.1	1 viol.	✓ Clean	`N[C@@H](Cc1ccc(O)c(-c2cc(C[C@H](N)C(=O)O)ccc2O)…`
ZINC6091882 ZINC	0.677	360.4 Da LogP 0.67 TPSA 167.1	1 viol.	✓ Clean	`N[C@@H](Cc1ccc(O)c(-c2cc(C[C@@H](N)C(=O)O)ccc2O…`
ZINC6091894 ZINC	0.677	360.4 Da LogP 0.67 TPSA 167.1	1 viol.	✓ Clean	`N[C@H](Cc1ccc(O)c(-c2cc(C[C@@H](N)C(=O)O)ccc2O)…`
ZINC113264413 ZINC	0.667	317.4 Da LogP 3.98 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(-c2ccc(-c3ccccc3)cc2)cc1)C(=O)O`
ZINC113264415 ZINC	0.667	317.4 Da LogP 3.98 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(-c2ccc(-c3ccccc3)cc2)cc1)C(=O)O`
ZINC14982778 ZINC	0.667	207.2 Da LogP 0.84 TPSA 80.4	✓ Ro5	✓ Clean	`CC(=O)c1ccc(C[C@@H](N)C(=O)O)cc1`
ZINC14982780 ZINC	0.667	207.2 Da LogP 0.84 TPSA 80.4	✓ Ro5	✓ Clean	`CC(=O)c1ccc(C[C@H](N)C(=O)O)cc1`
ZINC1569734 ZINC	0.667	238.2 Da LogP -0.54 TPSA 112.6	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(O)cc1)C(=O)NCC(=O)O`
ZINC2244337 ZINC	0.667	241.3 Da LogP 2.31 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(-c2ccccc2)cc1)C(=O)O`
ZINC2244338 ZINC	0.667	241.3 Da LogP 2.31 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(-c2ccccc2)cc1)C(=O)O`
ZINC2505456 ZINC	0.667	210.2 Da LogP 0.72 TPSA 94.8	✓ Ro5	✓ Clean	`O=C(O)C(Cc1ccc(O)cc1)C(=O)O`
ZINC2575475 ZINC	0.667	238.2 Da LogP -0.54 TPSA 112.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(O)cc1)C(=O)NCC(=O)O`
ZINC2575618 ZINC	0.667	208.2 Da LogP -0.26 TPSA 106.4	✓ Ro5	✓ Clean	`NC(=O)c1ccc(C[C@H](N)C(=O)O)cc1`
ZINC4241956 ZINC	0.667	208.2 Da LogP -0.26 TPSA 106.4	✓ Ro5	✓ Clean	`NC(=O)c1ccc(C[C@@H](N)C(=O)O)cc1`
ZINC2004481 ZINC	0.647	344.4 Da LogP 0.78 TPSA 132.9	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](Cc1ccc(O)cc1)…`
ZINC116924508 ZINC	0.645	215.2 Da LogP 1.58 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(C(F)F)cc1)C(=O)O`
ZINC116924543 ZINC	0.645	215.2 Da LogP 1.58 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(C(F)F)cc1)C(=O)O`
ZINC2385595 ZINC	0.645	207.3 Da LogP 1.76 TPSA 63.3	✓ Ro5	✓ Clean	`CC(C)c1ccc(C[C@H](N)C(=O)O)cc1`
ZINC2392305 ZINC	0.645	221.3 Da LogP 1.94 TPSA 63.3	✓ Ro5	✓ Clean	`CC(C)(C)c1ccc(C[C@H](N)C(=O)O)cc1`
ZINC2392306 ZINC	0.645	221.3 Da LogP 1.94 TPSA 63.3	✓ Ro5	✓ Clean	`CC(C)(C)c1ccc(C[C@@H](N)C(=O)O)cc1`
ZINC3679865 ZINC	0.645	207.3 Da LogP 1.76 TPSA 63.3	✓ Ro5	✓ Clean	`CC(C)c1ccc(C[C@@H](N)C(=O)O)cc1`
ZINC44283754 ZINC	0.645	207.3 Da LogP 1.59 TPSA 63.3	✓ Ro5	✓ Clean	`CCCc1ccc(C[C@H](N)C(=O)O)cc1`
ZINC44283756 ZINC	0.645	207.3 Da LogP 1.59 TPSA 63.3	✓ Ro5	✓ Clean	`CCCc1ccc(C[C@@H](N)C(=O)O)cc1`
ZINC44284738 ZINC	0.645	255.3 Da LogP 2.62 TPSA 63.3	✓ Ro5	✓ Clean	`Cc1ccc(-c2ccc(C[C@H](N)C(=O)O)cc2)cc1`
ZINC44284740 ZINC	0.645	255.3 Da LogP 2.62 TPSA 63.3	✓ Ro5	✓ Clean	`Cc1ccc(-c2ccc(C[C@@H](N)C(=O)O)cc2)cc1`
ZINC4763192 ZINC	0.636	271.3 Da LogP 2.01 TPSA 72.5	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(O)cc1)C(=O)OCc1ccccc1`
ZINC4763195 ZINC	0.636	271.3 Da LogP 2.01 TPSA 72.5	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(O)cc1)C(=O)OCc1ccccc1`
ZINC2566273 ZINC	0.629	252.3 Da LogP -0.15 TPSA 112.7	✓ Ro5	✓ Clean	`C[C@H](NC(=O)[C@@H](N)Cc1ccc(O)cc1)C(=O)O`
ZINC2566279 ZINC	0.629	252.3 Da LogP -0.15 TPSA 112.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(O)cc1)C(=O)NCCC(=O)O`
ZINC3590784 ZINC	0.629	252.3 Da LogP -0.15 TPSA 112.7	✓ Ro5	✓ Clean	`C[C@@H](NC(=O)[C@@H](N)Cc1ccc(O)cc1)C(=O)O`
ZINC4787311 ZINC	0.629	252.3 Da LogP -0.15 TPSA 112.7	✓ Ro5	✓ Clean	`C[C@H](NC(=O)[C@H](N)Cc1ccc(O)cc1)C(=O)O`
ZINC4787313 ZINC	0.629	252.3 Da LogP -0.15 TPSA 112.7	✓ Ro5	✓ Clean	`C[C@@H](NC(=O)[C@H](N)Cc1ccc(O)cc1)C(=O)O`
ZINC20112424 ZINC	0.625	259.2 Da LogP 0.32 TPSA 120.9	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(CP(=O)(O)O)cc1)C(=O)O`
ZINC2149429 ZINC	0.625	233.2 Da LogP 1.66 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(C(F)(F)F)cc1)C(=O)O`
ZINC2149431 ZINC	0.625	233.2 Da LogP 1.66 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(C(F)(F)F)cc1)C(=O)O`
ZINC3679854 ZINC	0.625	211.3 Da LogP 1.36 TPSA 63.3	✓ Ro5	✓ Clean	`CSc1ccc(C[C@@H](N)C(=O)O)cc1`
ZINC44284605 ZINC	0.625	275.7 Da LogP 2.96 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(-c2ccc(Cl)cc2)cc1)C(=O)O`

PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.